6eit

Coxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1

Method: ELECTRON MICROSCOPY Dmax: 108.6 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

VP1

OrganismNot specified

UniProt G3C8J7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain 1; UniProt 1–305 Not recorded VP2 × 60 (A0A088F913) VP3 × 60 (Q0GYP7) Intercellular adhesion molecule 1 × 60 (P05362) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2) cryo-EM vitrification conditions:Cryogen ETHANE;On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing Resolution 3.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name G3C8J7_9ENTO
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–305; UniProt 1–305

VP2

OrganismNot specified

UniProt A0A088F913

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain 2; UniProt 70–340 Not recorded VP1 × 60 (G3C8J7) VP3 × 60 (Q0GYP7) Intercellular adhesion molecule 1 × 60 (P05362) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2) cryo-EM vitrification conditions:Cryogen ETHANE;On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing Resolution 3.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A088F913_9ENTO
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–271; UniProt 70–340

VP3

OrganismNot specified

UniProt Q0GYP7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain 3; UniProt 341–580 Not recorded VP1 × 60 (G3C8J7) VP2 × 60 (A0A088F913) Intercellular adhesion molecule 1 × 60 (P05362) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2) cryo-EM vitrification conditions:Cryogen ETHANE;On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing Resolution 3.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q0GYP7_9ENTO
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–240; UniProt 341–580

Intercellular adhesion molecule 1

Homo sapiens

UniProt P05362

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 240 PDB declaration: 240-meric(240) Consistent with protein copy count Chain 4; UniProt 28–112 Not recorded VP1 × 60 (G3C8J7) VP2 × 60 (A0A088F913) VP3 × 60 (Q0GYP7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;TBS buffer (Coxsackievirus A24v) Phosphate buffer (ICAM-1 D1-D2) cryo-EM vitrification conditions:Cryogen ETHANE;On-grid binding of the receptor was performed by applying 3 microliters of ICAM-1 (9.85 mg/ml) to the pre-blotted, virus-containing grid, and leaving for 30 seconds before blotting and freezing Resolution 3.90 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

12 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ICAM1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain 4; PDBConstruct 1–85; UniProt 28–112

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6eit

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6eit
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6eit
Deposition date deposition_date2017-09-19
Structure title titleCoxsackievirus A24v in complex with the D1-D2 fragment of ICAM-1
Keywords keywordsEnterovirus, Receptor, Complex, picornavirus, VIRUS; VIRUS
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier32.03
Radius of gyration Rg (electron density) rg_electron31.36
Forward intensity I(0) i0143807000.00
Molecular weight molecular_weight95482.0 kDa
Excluded volume excluded_volume119430 ų
Envelope volume envelope_volume163600 ų
Hydration-shell volume shell_volume42999 ų
Envelope diameter envelope_diameter114.5
Shell Rg shell_rg38.33
Envelope Rg envelope_rg32.50
Shape Rg shape_rg31.33
Total Rg total_rg32.05
Total atoms total_atoms6717
Residues n_residues860
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax108.6
Rg (real space) rg_real31.99
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.4380e+08
I(0) uncertainty (real space) i0_real_error2.6420e+06
Rg (reciprocal space) rg_reciprocal32.01
I(0) (reciprocal space) i0_reciprocal143800000.0000
Solution quality estimate total_estimate0.8813
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.7
Skewness Skewness skewness0.329
Kurtosis Kurtosis kurtosis-0.290
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17890000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id6eit100
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id6eit200
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id6eit300
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily20
Domain ID domain_id6eit400
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)